Any feedback?
Literature summary extracted from
- Role of cysteine residues in the structure, stability, and alkane producing activity of cyanobacterial aldehyde deformylating oxygenase (2015), PLoS ONE, 10, e0122217 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.1.99.5 | recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)pLysS | Nostoc punctiforme |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.1.99.5 | C107A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
| 4.1.99.5 | C107A/C117A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
| 4.1.99.5 | C117A | site-directed mutagenesis, the mutation does not affect the hydrocarbon producing activity of the enzyme | Nostoc punctiforme |
| 4.1.99.5 | C71A | site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme | Nostoc punctiforme |
| 4.1.99.5 | C71A/C107A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
| 4.1.99.5 | C71A/C107A/C117A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
| 4.1.99.5 | C71A/C117A | site-directed mutagenesis, the mutant has reduced activity compared to wild-type, and an activity comparable to or even lower than the activity of the C71A variant | Nostoc punctiforme |
| 4.1.99.5 | C71S | site-directed mutagenesis, the mutant shows reduced hydrocarbon producing activity and facilitated formation of a dimer compared to wild-type enzyme | Nostoc punctiforme |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.1.99.5 | additional information | - |
additional information | Michaelis-Menten kinetics | Nostoc punctiforme |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.5 | Fe2+ | di-iron center, the amount of hydrocarbons produced in recombinant Escherichia coli is decreased when the iron concentration in the M9 medium is decreased. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme | Nostoc punctiforme |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Nostoc punctiforme | - |
an alkane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | Nostoc punctiforme ATCC 29133 / PCC 73102 | - |
an alkane + formate + H2O + 2 NADP+ | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.1.99.5 | Nostoc punctiforme | B2J1M1 | - |
- |
| 4.1.99.5 | Nostoc punctiforme ATCC 29133 / PCC 73102 | B2J1M1 | - |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 4.1.99.5 | recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography and dialysis | Nostoc punctiforme |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | an alkane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | a long-chain aldehyde + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | an alkane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | additional information | GC-MS measurements and identification of products | Nostoc punctiforme | ? | - |
? | |
| 4.1.99.5 | additional information | GC-MS measurements and identification of products | Nostoc punctiforme ATCC 29133 / PCC 73102 | ? | - |
? | |
| 4.1.99.5 | n-hexadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | pentadecane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | n-hexadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | pentadecane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | heptadecane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | n-octadecanal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | heptadecane + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | n-octadecenal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme | 1-heptadecene + formate + H2O + 2 NADP+ | - |
? | |
| 4.1.99.5 | n-octadecenal + O2 + 2 NADPH + 2 H+ | - |
Nostoc punctiforme ATCC 29133 / PCC 73102 | 1-heptadecene + formate + H2O + 2 NADP+ | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.1.99.5 | aldehyde deformylating oxygenase | - |
Nostoc punctiforme |
| 4.1.99.5 | Npun_R1711 | - |
Nostoc punctiforme |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.5 | 37 | - |
in vivo assay at | Nostoc punctiforme |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.1.99.5 | 43 | - |
Tm of recombinant mutant C107A/C117A | Nostoc punctiforme |
| 4.1.99.5 | 46 | - |
Tm of recombinant mutant C71S | Nostoc punctiforme |
| 4.1.99.5 | 47 | - |
Tm of recombinant mutants C71A, C107A, C117A, and C71A/C117A | Nostoc punctiforme |
| 4.1.99.5 | 48 | - |
Tm of recombinant mutant C71A/C107A | Nostoc punctiforme |
| 4.1.99.5 | 53 | - |
Tm of recombinant wild-type | Nostoc punctiforme |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.1.99.5 | NADPH | - |
Nostoc punctiforme | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 4.1.99.5 | malfunction | C71A/S mutations reduce the hydrocarbon producing activity of AD and facilitate the formation of a dimer, while mutations at Cys107 and Cys117 do not affect the hydrocarbon producing activity of the enzyme. The Cys-to-Ala/Ser mutations do not affect the iron binding to the enzyme. Structural features of the Cys-deficient mutants, overview | Nostoc punctiforme |
| 4.1.99.5 | additional information | Cys71, which is located in close proximity to the substrate-binding site, plays a crucial role in maintaining the activity, structure, and stability of the enzyme | Nostoc punctiforme |
| 4.1.99.5 | physiological function | aldehyde deformylating oxygenase is a key enzyme for alkane biosynthesis in cyanobacteria | Nostoc punctiforme |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
